MolNFT v1 · #90365 · protein

Human P38 MAP kinase in complex with np-F4 and RL87

4EH5 · Mitogen-activated protein kinase 14: “Human P38 MAP kinase in complex with np-F4 and RL87”. X-ray diffraction, 2 ligands (IRG, 0OM), 6 pockets (best druggability 0.69). MolNFT v1 #90365 on GenesisL1: 3D structure, binding sites and…

PDB: 4EH5
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 14
EC: 2.7.11.24
UniProt: Q16539
Ligands: IRG, 0OM
Pockets: 6 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	329	39% helix, 16% strand	Q16539

Ligands and binding sites

IRG · N~4~-cyclopropyl-2-phenylquinazoline-4,7-diamine · ligand · chains A
0OM · benzyl pyridine-3-carboxylate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	488	0.69	0.79	49	0OM
2	129	0.66	0.88	20	IRG
3	130	0.44	0.76	26	empty
4	106	0.38	0.75	19	empty
5	81	0.36	0.75	16	empty

Compared structures

4EH5 · Human p38 MAP kinase in complex with NP-F4 and RL87 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q16539
Elsewhere: RCSB PDB 4EH5 · PDBe 4EH5 · UniProt Q16539

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